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Updated: Jul 19, 2026

Production of Nurr-1 Specific Polyclonal Antibodies Free of Cross-reactivity Against Its Close Homologs, Nor1 and Nur77
Published on: August 17, 2015
Post-translational control of Nur77
1MRC Protein Phosphorylation Unit, University of Dundee, Dundee DD1 5EH, Scotland, UK. a.d.wingate@dundee.ac.uk
Abstract:
Nur77 is a nuclear orphan receptor that has been implicated in both cell survival and apoptosis. With the exception of T-cells, translocation of Nur77 to the cytoplasm promotes cell death, while its retention in the nucleus promotes survival and proliferation. Nur77 appears to be a true orphan receptor, indicating that its activity must be controlled by ligand-independent mechanisms. Here, we discuss the role of phosphorylation in the regulation of Nur77.
Insights
Nur77, a nuclear orphan receptor, regulates cell survival and apoptosis. Phosphorylation is a key ligand-independent mechanism controlling Nur77
Area of Science:
- Molecular biology
- Cellular signaling
Background:
- Nur77 is a nuclear orphan receptor involved in cell survival and apoptosis.
- Cytoplasmic translocation of Nur77 induces cell death, while nuclear retention promotes survival.
- Nur77 activity is regulated by ligand-independent mechanisms.
Purpose of the Study:
- To discuss the role of phosphorylation in Nur77 regulation.
Main Methods:
- Literature review and discussion of existing research on Nur77 phosphorylation.
Main Results:
- Phosphorylation is identified as a critical mechanism for regulating Nur77's function.
- Specific phosphorylation events influence Nur77's subcellular localization and downstream effects.
Conclusions:
- Phosphorylation plays a crucial role in controlling Nur77-mediated cell survival and apoptosis pathways.
- Understanding Nur77 phosphorylation offers insights into cellular fate determination.
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